Evidence map›Paper›PMID 19084524›Full record

ArticleFEBS letters2009

Reductive dioxygen scavenging by flavo-diiron proteins of Clostridium acetobutylicum.

Falk Hillmann, Oliver Riebe, Ralf-Jörg Fischer, Augustin Mot, Jonathan D Caranto, Donald M Kurtz, Hubert Bahl

Open access · bronzeAbstract read
In one paragraph

Article in FEBS letters, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 47 citations in OpenAlex.

  1. On the diversity of FProteins · 2021
    Article
  2. Article
  3. Article
  4. Article
  5. The dual function of flavodiiron proteins: oxygen and/or nitric oxide reductases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Review
  6. Thiol-based redox switches in prokaryotes.Biological chemistry · 2015
    Review
  7. Dioxygen and nitric oxide scavenging by Treponema denticola flavodiiron protein: a mechanistic paradigm for catalysis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Histidine ligand variants of a flavo-diiron protein: effects on structure and activities.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 3 countries.

Falk HillmannDivision of Microbiology, Institute of Biological Sciences, University of Rostock, Rostock, Germany.
Oliver Riebe
Ralf-Jörg Fischer
Augustin Mot
Jonathan D Caranto
Donald M Kurtz
Hubert Bahl
University of Rostock · DEThe University of Texas at San Antonio · US

Funding

Kurtz NIHR01GM040388 · NIGMS · UNIVERSITY OF TEXAS SAN ANTONIO · PI KURTZ, DONALD M. · 1988 to 2014
$4.2M
NIGMS NIH HHS GM040388NIGMS NIH HHS R01 GM040388
6 · The paper itself

Abstract

Two flavo-diiron proteins (FDPs), FprA1 and FprA2, are up-regulated when the strictly anaerobic solvent producer, Clostridium acetobutylicum, is exposed to dioxygen. These two FDPs were purified following heterologous overexpression in Escherichia coli as N-terminal Strep-tag fusion proteins. The recombinant FprA1 and FprA2 were found to be homodimeric and homotetrameric, respectively, and both FDPs functioned as terminal components of NADH oxidases (NADH:O(2) oxidoreductases) when using C. acetobutylicum NADH:rubredoxin oxidoreductase (NROR) and rubredoxin (Rd) as electron transport intermediaries. Both FDPs catalyzed the four-electron reduction of molecular oxygen to water with similar specific activities. The results are consistent with these FDPs functioning as efficient scavengers of intracellular dioxygen under aerobic or microoxic growth conditions.

Indexed as

Amino Acid SequenceClostridium acetobutylicumDimerizationEscherichia coliFlavoproteinsMolecular Sequence DataNADH, NADPH OxidoreductasesNitric OxideOxidation-ReductionOxygenRecombinant ProteinsRubredoxinsFlavoproteinsNADH, NADPH OxidoreductasesNitric OxideOxygenRecombinant Proteinsrubredoxin-NAD+ reductaseRubredoxins

Identifiers

PMID19084524
PMCPMC2629652
OpenAlexW2046654873

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.